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Literature summary for 1.6.2.2 extracted from

  • Bagnaresi, P.; Mazars-Marty, D.; Pupilld, P.; Marty, F.; Briat, J.F.
    Tonoplast subcellular localization of maize cytochrome b5 reductases (2000), Plant J., 24, 645-654.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomaces cerevisiae Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
tonoplast
-
Zea mays
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome b5 + NADH Zea mays enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals 2 ferrocytochrome b5 + NAD+ + H+
-
?

Organism

Organism UniProt Comment Textmining
Zea mays Q8W2K4
-
-

Source Tissue

Source Tissue Comment Organism Textmining
root
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome b5 + NADH enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals Zea mays 2 ferrocytochrome b5 + NAD+ + H+
-
?
2 ferricytochrome c + NADH isoforms I and II, 16% and 27% of Fe3+-citrate reduction respectively Zea mays 2 ferrocytochrome c + NAD+ + H+
-
?
Cu2+-citrate + NADH isoforms I and II, 59 and 47% of Fe3+-citrate reduction respectively Zea mays Cu+-citrate + NAD+
-
?
Fe3+-citrate + NADH isoforms I and II Zea mays Fe2+-citrate + NAD+
-
?
Fe3+-EDTA + NADH isoforms I and II Zea mays Fe2+-EDTA + NAD+
-
?